MolNFT v1 · #20290 · protein
Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 ångströms resolution: implications for atcase mutants and the mechanism of negative cooperativity
1RAD: “Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 ångströms resolution…”. X-ray diffraction. MolNFT v1 #20290 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1RAD
- Type
- protein
- Length
- 926 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A786, P0A7F3
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 310 | — | P0A786 |
| B, D | — | protein | 153 | — | P0A7F3 |
Compared structures
- 1RAD · Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 ångströms… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A786 · AlphaFold monomer V2.0 prediction for aspartate carbamoyltransferase catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.97
- P0A7F3 · AlphaFold monomer V2.0 prediction for aspartate carbamoyltransferase regulatory chain… · a predicted model of the same protein · chain B against A, TM-score 0.91
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P0A786
- Every structure of UniProt P0A7F3
- Elsewhere: RCSB PDB 1RAD · PDBe 1RAD · UniProt P0A786 · UniProt P0A7F3
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